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DGAT1_ARATH
ID   DGAT1_ARATH             Reviewed;         520 AA.
AC   Q9SLD2; Q9S7F2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305};
DE            Short=AtDGAT1 {ECO:0000303|PubMed:23770095};
DE            EC=2.3.1.20 {ECO:0000269|PubMed:11171171};
DE   AltName: Full=Protein TRIACYLGLYCEROL 1 {ECO:0000303|PubMed:10580283};
GN   Name=DGAT1 {ECO:0000303|PubMed:12177474};
GN   Synonyms=ABX45 {ECO:0000303|PubMed:10580283},
GN   DAGAT {ECO:0000312|EMBL:AAF19262.1}, TAG1 {ECO:0000303|PubMed:10571850,
GN   ECO:0000303|PubMed:10580283}; OrderedLocusNames=At2g19450;
GN   ORFNames=F3P11.5;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=10386579; DOI=10.1016/s0014-5793(99)00646-8;
RA   Hobbs D.H., Lu C., Hills M.J.;
RT   "Cloning of a cDNA encoding diacylglycerol acyltransferase from Arabidopsis
RT   thaliana and its functional expression.";
RL   FEBS Lett. 452:145-149(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLN-130, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10571850; DOI=10.1046/j.1365-313x.1999.00555.x;
RA   Zou J., Wei Y., Jako C., Kumar A., Selvaraj G., Taylor D.C.;
RT   "The Arabidopsis thaliana TAG1 mutant has a mutation in a diacylglycerol
RT   acyltransferase gene.";
RL   Plant J. 19:645-653(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=10580283; DOI=10.1016/s0981-9428(99)00115-1;
RA   Routaboul J.M., Benning C., Bechtold N., Caboche M., Lepiniec L.;
RT   "The TAG1 locus of Arabidopsis encodes for a diacylglycerol
RT   acyltransferase.";
RL   Plant Physiol. Biochem. 37:831-840(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=10601854; DOI=10.1046/j.1432-1327.2000.00961.x;
RA   Bouvier-Nave P., Benveniste P., Oelkers P., Sturley S.L., Schaller H.;
RT   "Expression in yeast and tobacco of plant cDNAs encoding acyl
RT   CoA:diacylglycerol acyltransferase.";
RL   Eur. J. Biochem. 267:85-96(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [8]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=11171171; DOI=10.1042/bst0280687;
RA   Hobbs D.H., Hills M.J.;
RT   "Expression and characterization of diacylglycerol acyltransferase from
RT   Arabidopsis thaliana in insect cell cultures.";
RL   Biochem. Soc. Trans. 28:687-689(2000).
RN   [9]
RP   FUNCTION.
RX   PubMed=11402213; DOI=10.1104/pp.126.2.861;
RA   Jako C., Kumar A., Wei Y., Zou J., Barton D.L., Giblin E.M., Covello P.S.,
RA   Taylor D.C.;
RT   "Seed-specific over-expression of an Arabidopsis cDNA encoding a
RT   diacylglycerol acyltransferase enhances seed oil content and seed weight.";
RL   Plant Physiol. 126:861-874(2001).
RN   [10]
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=12177474; DOI=10.1104/pp.003087;
RA   Kaup M.T., Froese C.D., Thompson J.E.;
RT   "A role for diacylglycerol acyltransferase during leaf senescence.";
RL   Plant Physiol. 129:1616-1626(2002).
RN   [11]
RP   FUNCTION.
RX   PubMed=12114588; DOI=10.1104/pp.006122;
RA   Lu C., Hills M.J.;
RT   "Arabidopsis mutants deficient in diacylglycerol acyltransferase display
RT   increased sensitivity to abscisic acid, sugars, and osmotic stress during
RT   germination and seedling development.";
RL   Plant Physiol. 129:1352-1358(2002).
RN   [12]
RP   TISSUE SPECIFICITY, AND INDUCTION BY GLUCOSE.
RX   PubMed=12825687; DOI=10.1023/a:1023935605864;
RA   Lu C.L., de Noyer S.B., Hobbs D.H., Kang J., Wen Y., Krachtus D.,
RA   Hills M.J.;
RT   "Expression pattern of diacylglycerol acyltransferase-1, an enzyme involved
RT   in triacylglycerol biosynthesis, in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 52:31-41(2003).
RN   [13]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=20040537; DOI=10.1105/tpc.109.071795;
RA   Zhang M., Fan J., Taylor D.C., Ohlrogge J.B.;
RT   "DGAT1 and PDAT1 acyltransferases have overlapping functions in Arabidopsis
RT   triacylglycerol biosynthesis and are essential for normal pollen and seed
RT   development.";
RL   Plant Cell 21:3885-3901(2009).
RN   [14]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=20101470; DOI=10.1007/s11745-010-3385-4;
RA   Li R., Yu K., Hildebrand D.F.;
RT   "DGAT1, DGAT2 and PDAT expression in seeds and other tissues of epoxy and
RT   hydroxy fatty acid accumulating plants.";
RL   Lipids 45:145-157(2010).
RN   [15]
RP   INDUCTION.
RX   PubMed=23942253; DOI=10.1016/j.febslet.2013.07.045;
RA   Kong Y., Chen S., Yang Y., An C.;
RT   "ABA-insensitive (ABI) 4 and ABI5 synergistically regulate DGAT1 expression
RT   in Arabidopsis seedlings under stress.";
RL   FEBS Lett. 587:3076-3082(2013).
RN   [16]
RP   FUNCTION.
RX   PubMed=23770095; DOI=10.1016/j.febslet.2013.06.003;
RA   Zhou X.R., Shrestha P., Yin F., Petrie J.R., Singh S.P.;
RT   "AtDGAT2 is a functional acyl-CoA:diacylglycerol acyltransferase and
RT   displays different acyl-CoA substrate preferences than AtDGAT1.";
RL   FEBS Lett. 587:2371-2376(2013).
RN   [17]
RP   INTERACTION WITH LPCAT2 AND LPAT2.
RC   STRAIN=cv. Columbia;
RX   PubMed=26586834; DOI=10.1104/pp.15.01563;
RA   Shockey J., Regmi A., Cotton K., Adhikari N., Browse J., Bates P.D.;
RT   "Identification of Arabidopsis GPAT9 (At5g60620) as an essential gene
RT   involved in triacylglycerol biosynthesis.";
RL   Plant Physiol. 170:163-179(2016).
CC   -!- FUNCTION: Major contributor to triacylglycerol (TAG) synthesis and oil
CC       accumulation in seeds. Catalyzes the acylation of the sn-3 hydroxy
CC       group of sn-1,2-diacylglycerol using acyl-CoA (PubMed:10571850,
CC       PubMed:10580283, PubMed:10601854, PubMed:11402213, PubMed:12114588,
CC       PubMed:20040537, PubMed:20101470). Can use palmitoyl-CoA and oleoyl-CoA
CC       as substrates (PubMed:20101470). Can use oleoyl-CoA and linoleoyl-CoA
CC       as substrates. Has substrate preference for oleoyl-CoA compared to
CC       linoleoyl-CoA (PubMed:23770095). Has complementary functions with PDAT1
CC       that are essential for triacylglycerol synthesis and normal development
CC       of both seeds and pollen (PubMed:20040537).
CC       {ECO:0000269|PubMed:10571850, ECO:0000269|PubMed:10580283,
CC       ECO:0000269|PubMed:10601854, ECO:0000269|PubMed:11402213,
CC       ECO:0000269|PubMed:12114588, ECO:0000269|PubMed:20040537,
CC       ECO:0000269|PubMed:20101470, ECO:0000269|PubMed:23770095}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC         + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC         Evidence={ECO:0000269|PubMed:11171171};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC         Evidence={ECO:0000269|PubMed:11171171};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol =
CC         1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:10386579};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC         Evidence={ECO:0000269|PubMed:10386579};
CC   -!- ACTIVITY REGULATION: Partially inhibited by niacin.
CC       {ECO:0000269|PubMed:11171171}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is between 6.75-7.25. {ECO:0000269|PubMed:11171171};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- SUBUNIT: Interacts with LPCAT2 and LPAT2.
CC       {ECO:0000269|PubMed:26586834}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:12177474}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:12177474}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12177474}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:12177474}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in young developing
CC       seeds. {ECO:0000269|PubMed:10571850, ECO:0000269|PubMed:12825687,
CC       ECO:0000269|PubMed:20040537, ECO:0000269|PubMed:20101470}.
CC   -!- DEVELOPMENTAL STAGE: Peak of expression in seeds 15 days after
CC       flowering. Highly expressed in senescing leaves.
CC       {ECO:0000269|PubMed:12177474, ECO:0000269|PubMed:20101470}.
CC   -!- INDUCTION: Up-regulated by glucose (PubMed:12825687). Induced by
CC       abscisic acid (ABA), jasmonate, salicylate, salt and osmotic stress
CC       (PubMed:23942253). {ECO:0000269|PubMed:12825687,
CC       ECO:0000269|PubMed:23942253}.
CC   -!- DISRUPTION PHENOTYPE: Decreased oil content and modified size and shape
CC       of oil bodies. {ECO:0000269|PubMed:20040537}.
CC   -!- MISCELLANEOUS: The AS11 mutant has a complete duplication of exon 2.
CC   -!- MISCELLANEOUS: DGAT1 deficiency alters carbohydrate metabolism.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR   EMBL; AJ131831; CAB44774.1; -; mRNA.
DR   EMBL; AJ238008; CAB45373.1; -; mRNA.
DR   EMBL; AF051849; AAF19262.1; -; mRNA.
DR   EMBL; AC003058; AAM14875.1; -; Genomic_DNA.
DR   EMBL; AC005917; AAD10144.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06882.1; -; Genomic_DNA.
DR   EMBL; AY054480; AAK96671.1; -; mRNA.
DR   EMBL; BT008883; AAP68322.1; -; mRNA.
DR   PIR; H84576; H84576.
DR   PIR; T01293; T01293.
DR   PIR; T01294; T01294.
DR   PIR; T52584; T52584.
DR   RefSeq; NP_179535.1; NM_127503.3.
DR   AlphaFoldDB; Q9SLD2; -.
DR   SMR; Q9SLD2; -.
DR   BioGRID; 1819; 1.
DR   IntAct; Q9SLD2; 1.
DR   STRING; 3702.AT2G19450.1; -.
DR   SwissLipids; SLP:000001794; -.
DR   iPTMnet; Q9SLD2; -.
DR   PaxDb; Q9SLD2; -.
DR   PRIDE; Q9SLD2; -.
DR   ProteomicsDB; 224212; -.
DR   EnsemblPlants; AT2G19450.1; AT2G19450.1; AT2G19450.
DR   GeneID; 816464; -.
DR   Gramene; AT2G19450.1; AT2G19450.1; AT2G19450.
DR   KEGG; ath:AT2G19450; -.
DR   Araport; AT2G19450; -.
DR   TAIR; locus:2047665; AT2G19450.
DR   eggNOG; KOG0380; Eukaryota.
DR   HOGENOM; CLU_018190_0_1_1; -.
DR   InParanoid; Q9SLD2; -.
DR   OMA; HAIIVWL; -.
DR   OrthoDB; 1275897at2759; -.
DR   PhylomeDB; Q9SLD2; -.
DR   BioCyc; MetaCyc:MON-2081; -.
DR   BRENDA; 2.3.1.20; 399.
DR   UniPathway; UPA00282; -.
DR   PRO; PR:Q9SLD2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SLD2; baseline and differential.
DR   Genevisible; Q9SLD2; AT.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IDA:TAIR.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:TAIR.
DR   GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0007568; P:aging; IEP:TAIR.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; TAS:TAIR.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010030; P:positive regulation of seed germination; IMP:TAIR.
DR   GO; GO:0045995; P:regulation of embryonic development; IMP:TAIR.
DR   GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR   GO; GO:0009409; P:response to cold; IMP:TAIR.
DR   GO; GO:0009749; P:response to glucose; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IDA:TAIR.
DR   InterPro; IPR027251; Diacylglycerol_acylTrfase1.
DR   InterPro; IPR004299; MBOAT_fam.
DR   InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR   PANTHER; PTHR10408; PTHR10408; 1.
DR   Pfam; PF03062; MBOAT; 1.
DR   PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
DR   PIRSF; PIRSF500231; Oat_dag; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Chloroplast; Endoplasmic reticulum; Glycerol metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Plastid;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..520
FT                   /note="Diacylglycerol O-acyltransferase 1"
FT                   /id="PRO_0000398613"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          28..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           392..398
FT                   /note="FYXDWWN motif"
FT                   /evidence="ECO:0000250|UniProtKB:O75907"
FT   COMPBIAS        35..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        447
FT                   /evidence="ECO:0000250|UniProtKB:O75907"
FT   MUTAGEN         130
FT                   /note="Q->QSHAGLFNLCVVVLIAVNSRLIIENLMK: In AS11; strong
FT                   reduction of enzymatic activity and delayed seed
FT                   development."
FT                   /evidence="ECO:0000269|PubMed:10571850"
SQ   SEQUENCE   520 AA;  58986 MW;  9CD0E3E8956CEFF4 CRC64;
     MAILDSAGVT TVTENGGGEF VDLDRLRRRK SRSDSSNGLL LSGSDNNSPS DDVGAPADVR
     DRIDSVVNDD AQGTANLAGD NNGGGDNNGG GRGGGEGRGN ADATFTYRPS VPAHRRARES
     PLSSDAIFKQ SHAGLFNLCV VVLIAVNSRL IIENLMKYGW LIRTDFWFSS RSLRDWPLFM
     CCISLSIFPL AAFTVEKLVL QKYISEPVVI FLHIIITMTE VLYPVYVTLR CDSAFLSGVT
     LMLLTCIVWL KLVSYAHTSY DIRSLANAAD KANPEVSYYV SLKSLAYFMV APTLCYQPSY
     PRSACIRKGW VARQFAKLVI FTGFMGFIIE QYINPIVRNS KHPLKGDLLY AIERVLKLSV
     PNLYVWLCMF YCFFHLWLNI LAELLCFGDR EFYKDWWNAK SVGDYWRMWN MPVHKWMVRH
     IYFPCLRSKI PKTLAIIIAF LVSAVFHELC IAVPCRLFKL WAFLGIMFQV PLVFITNYLQ
     ERFGSTVGNM IFWFIFCIFG QPMCVLLYYH DLMNRKGSMS
 
 
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